Linked Life Data

3882426

Source:http://linkedlifedata.com/resource/pubmed/id/3882426

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-4-9
pubmed:abstractText
The complete amino acid sequence (121 residues) of histone H2B from gonads of the starfish Asterias rubens has been established from structural data obtained essentially from large fragments generated by cleavage of histone H2B at aspartyl residues and by limited hydrolysis of the dimer H2A-H2B with mouse submaxillary gland protease. No real sequence homology can be found between the amino-terminal sequence (residues 1-21) of starfish and calf H2B. One non-conservative substitution (serine-32 in calf----lysine-28 in starfish) leads to the presence of a cluster of eight basic residues (sequence 23-30) and to the disappearance of a potential site of phosphorylation. A particular structural feature of starfish histone H2B is the presence of N-dimethylproline at its amino-terminal end. By comparison with N-terminal acetylation, which is commonly found in histones, N-terminal methylation is rarely observed. At the present time the functional significance of the N-terminal methylation as well as that of the proline-rich nature of the amino-terminal sequence of the starfish histone H2B remain to be defined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
147
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
351-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Primary structure of histone H2B from gonads of the starfish Asterias rubens. Identification of an N-dimethylproline residue at the amino-terminal.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't